메뉴 건너뛰기




Volumn 20, Issue 3-4, 2007, Pages 467-483

Bioinformatic analysis of the TonB protein family

Author keywords

Gram negative bacteria; Iron transport; Multiple sequence alignment; TonB

Indexed keywords

BACTERIAL PROTEIN; CYANOCOBALAMIN; IRON COMPLEX; PROTEIN MECR1; PROTEIN TONB; UNCLASSIFIED DRUG;

EID: 34248636774     PISSN: 09660844     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10534-006-9049-4     Document Type: Conference Paper
Times cited : (59)

References (51)
  • 1
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25:3389-3402
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3
  • 2
    • 0842348747 scopus 로고    scopus 로고
    • Two TonB systems in Actinobacillus pleuropneumoniae: Their roles in iron acquisition and virulence
    • Beddek AJ, Sheehan BJ, Bosse JT et al. (2004) Two TonB systems in Actinobacillus pleuropneumoniae: their roles in iron acquisition and virulence. Infect Immun 72:701-708
    • (2004) Infect Immun , vol.72 , pp. 701-708
    • Beddek, A.J.1    Sheehan, B.J.2    Bosse, J.T.3
  • 3
    • 0036367233 scopus 로고    scopus 로고
    • Factors influencing methicillin resistance in staphylococci
    • Berger-Bachi B, Rohrer S (2002) Factors influencing methicillin resistance in staphylococci. Arch Microbiol 178:165-171
    • (2002) Arch Microbiol , vol.178 , pp. 165-171
    • Berger-Bachi, B.1    Rohrer, S.2
  • 4
    • 7444226402 scopus 로고    scopus 로고
    • X-ray crystal structure of the acylated beta-lactam sensor domain of BlaR1 from Staphylococcus aureus and the mechanism of receptor activation for signal transduction
    • Birck C, Cha JY, Cross J et al. (2004) X-ray crystal structure of the acylated beta-lactam sensor domain of BlaR1 from Staphylococcus aureus and the mechanism of receptor activation for signal transduction. J Am Chem Soc 126:13945-13947
    • (2004) J Am Chem Soc , vol.126 , pp. 13945-13947
    • Birck, C.1    Cha, J.Y.2    Cross, J.3
  • 5
    • 0036216270 scopus 로고    scopus 로고
    • Active transport of iron and siderophore antibiotics
    • Braun V, Braun M (2002) Active transport of iron and siderophore antibiotics. Curr Opin Microbiol 5:194-201
    • (2002) Curr Opin Microbiol , vol.5 , pp. 194-201
    • Braun, V.1    Braun, M.2
  • 6
    • 0025604251 scopus 로고
    • Structure and function of X-Pro dipeptide repeats in the TonB proteins of Salmonella typhimurium and Escherichia coli
    • Brewer S, Tolley M, Trayer IP et al. (1990) Structure and function of X-Pro dipeptide repeats in the TonB proteins of Salmonella typhimurium and Escherichia coli. J Mol Biol 216:883-895
    • (1990) J Mol Biol , vol.216 , pp. 883-895
    • Brewer, S.1    Tolley, M.2    Trayer, I.P.3
  • 7
    • 33644787225 scopus 로고    scopus 로고
    • Phage display reveals multiple contact sites between FhuA, an outer membrane receptor of Escherichia coli, and TonB
    • Carter DM, Gagnon JN, Damlaj M et al. (2006a) Phage display reveals multiple contact sites between FhuA, an outer membrane receptor of Escherichia coli, and TonB. J Mol Biol 357:236-251
    • (2006) J Mol Biol , vol.357 , pp. 236-251
    • Carter, D.M.1    Gagnon, J.N.2    Damlaj, M.3
  • 8
    • 33845951159 scopus 로고    scopus 로고
    • Interactions between TonB from Escherichia coli and the periplasmic protein FhuD
    • Carter DM, Miousse IR, Gagnon JN et al. (2006b) Interactions between TonB from Escherichia coli and the periplasmic protein FhuD. J Biol Chem
    • (2006) J Biol Chem
    • Carter, D.M.1    Miousse, I.R.2    Gagnon, J.N.3
  • 9
    • 0035920228 scopus 로고    scopus 로고
    • Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold
    • Chang C, Mooser A, Pluckthun A, Wlodawer A (2001) Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold. J Biol Chem 276:27535-27540
    • (2001) J Biol Chem , vol.276 , pp. 27535-27540
    • Chang, C.1    Mooser, A.2    Pluckthun, A.3    Wlodawer, A.4
  • 10
    • 16344373729 scopus 로고    scopus 로고
    • Comparative structural analysis of TonB-dependent outer membrane transporters: Implications for the transport cycle
    • Chimento DP, Kadner RJ, Wiener MC (2005) Comparative structural analysis of TonB-dependent outer membrane transporters: implications for the transport cycle. Proteins 59:240-251
    • (2005) Proteins , vol.59 , pp. 240-251
    • Chimento, D.P.1    Kadner, R.J.2    Wiener, M.C.3
  • 11
    • 0034663597 scopus 로고    scopus 로고
    • Application of multiple sequence alignment profiles to improve protein secondary structure prediction
    • Cuff JA, Barton GJ (2000) Application of multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins 40:502-511
    • (2000) Proteins , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 12
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, Grzesiek S, Vuister GW et al. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277-293
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3
  • 13
    • 24044525255 scopus 로고    scopus 로고
    • Siderophore transport through Escherichia coli outer membrane receptor FhuA with disulfide-tethered cork and barrel domains
    • Eisenhauer HA, Shames S, Pawelek PD, Coulton JW (2005) Siderophore transport through Escherichia coli outer membrane receptor FhuA with disulfide-tethered cork and barrel domains. J Biol Chem 280:30574-30580
    • (2005) J Biol Chem , vol.280 , pp. 30574-30580
    • Eisenhauer, H.A.1    Shames, S.2    Pawelek, P.D.3    Coulton, J.W.4
  • 15
    • 0346334403 scopus 로고    scopus 로고
    • Evidence for dynamic clustering of carboxy-terminal aromatic amino acids in TonB-dependent energy transduction
    • Ghosh J, Postle K (2004) Evidence for dynamic clustering of carboxy-terminal aromatic amino acids in TonB-dependent energy transduction. Mol Microbiol 51:203-213
    • (2004) Mol Microbiol , vol.51 , pp. 203-213
    • Ghosh, J.1    Postle, K.2
  • 16
    • 1842689851 scopus 로고    scopus 로고
    • Evidence of an intramolecular interaction between the two domains of the BlaR1 penicillin receptor during the signal transduction
    • Hanique S, Colombo ML, Goormaghtigh E et al. (2004) Evidence of an intramolecular interaction between the two domains of the BlaR1 penicillin receptor during the signal transduction. J Biol Chem 279:14264-14272
    • (2004) J Biol Chem , vol.279 , pp. 14264-14272
    • Hanique, S.1    Colombo, M.L.2    Goormaghtigh, E.3
  • 17
    • 0031033660 scopus 로고    scopus 로고
    • The penicillin sensory transducer, BlaR, involved in the inducibility of beta-lactamase synthesis in Bacillus licheniformis is embedded in the plasma membrane via a four-alpha-helix bundle
    • Hardt K, Joris B, Lepage S et al. (1997) The penicillin sensory transducer, BlaR, involved in the inducibility of beta-lactamase synthesis in Bacillus licheniformis is embedded in the plasma membrane via a four-alpha-helix bundle. Mol Microbiol 23:935-944
    • (1997) Mol Microbiol , vol.23 , pp. 935-944
    • Hardt, K.1    Joris, B.2    Lepage, S.3
  • 18
    • 0036231227 scopus 로고    scopus 로고
    • Quantification of known components of the Escherichia coli TonB energy transduction system: TonB, ExbB, ExbD and FepA
    • Higgs PI, Larsen RA, Postle K (2002) Quantification of known components of the Escherichia coli TonB energy transduction system: TonB, ExbB, ExbD and FepA. Mol Microbiol 44:271-281
    • (2002) Mol Microbiol , vol.44 , pp. 271-281
    • Higgs, P.I.1    Larsen, R.A.2    Postle, K.3
  • 19
    • 34249765651 scopus 로고
    • NMRView-a computer program for the visualization and analysis of NMR data
    • Johnson BA, Blevins RA (1994) NMRView-a computer program for the visualization and analysis of NMR data. J Biomol NMR 4:603-614
    • (1994) J Biomol NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 20
    • 0030841393 scopus 로고    scopus 로고
    • Iron, infections, and anemia of inflammation
    • Jurado RL (1997) Iron, infections, and anemia of inflammation. Clin Infect Dis 25:888-895
    • (1997) Clin Infect Dis , vol.25 , pp. 888-895
    • Jurado, R.L.1
  • 21
    • 0026723111 scopus 로고
    • Membrane topology of the Escherichia coli ExbD protein
    • Kampfenkel K, Braun V (1992) Membrane topology of the Escherichia coli ExbD protein. J Bacteriol 174:5485-5487
    • (1992) J Bacteriol , vol.174 , pp. 5485-5487
    • Kampfenkel, K.1    Braun, V.2
  • 22
    • 0027466914 scopus 로고
    • Topology of the ExbB protein in the cytoplasmic membrane of Escherichia coli
    • Kampfenkel K, Braun V (1993) Topology of the ExbB protein in the cytoplasmic membrane of Escherichia coli. J Biol Chem 268:6050-6057
    • (1993) J Biol Chem , vol.268 , pp. 6050-6057
    • Kampfenkel, K.1    Braun, V.2
  • 23
    • 0027154838 scopus 로고
    • A sequence-specific function for the N-terminal signal-like sequence of the TonB protein
    • Karlsson M, Hannavy K, Higgins CF (1993) A sequence-specific function for the N-terminal signal-like sequence of the TonB protein. Mol Microbiol 8:379-388
    • (1993) Mol Microbiol , vol.8 , pp. 379-388
    • Karlsson, M.1    Hannavy, K.2    Higgins, C.F.3
  • 24
    • 0024449503 scopus 로고
    • Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • Kay LE, Torchia DA, Bax A (1989) Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry 28:8972-8979
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 25
    • 1542320184 scopus 로고    scopus 로고
    • Enhanced binding of TonB to a ligand-loaded outer membrane receptor: Role of the oligomeric state of TonB in formation of a functional FhuA-TonB complex
    • Khursigara CM, De Crescenzo G, Pawelek PD, Coulton JW (2004) Enhanced binding of TonB to a ligand-loaded outer membrane receptor: role of the oligomeric state of TonB in formation of a functional FhuA-TonB complex. J Biol Chem 279:7405-7412
    • (2004) J Biol Chem , vol.279 , pp. 7405-7412
    • Khursigara, C.M.1    De Crescenzo, G.2    Pawelek, P.D.3    Coulton, J.W.4
  • 26
    • 17744372268 scopus 로고    scopus 로고
    • Deletion of the proline-rich region of TonB disrupts formation of a 2:1 complex with FhuA, an outer membrane receptor of Escherichia coli
    • Khursigara CM, De Crescenzo G, Pawelek PD, Coulton JW (2005) Deletion of the proline-rich region of TonB disrupts formation of a 2:1 complex with FhuA, an outer membrane receptor of Escherichia coli. Protein Sci 14:1266-1273
    • (2005) Protein Sci , vol.14 , pp. 1266-1273
    • Khursigara, C.M.1    De Crescenzo, G.2    Pawelek, P.D.3    Coulton, J.W.4
  • 27
    • 3142688448 scopus 로고    scopus 로고
    • Three paradoxes of ferric enterobactin uptake
    • Klebba PE (2003) Three paradoxes of ferric enterobactin uptake. Front Biosci 8:s1422-s1436
    • (2003) Front Biosci , vol.8
    • Klebba, P.E.1
  • 28
    • 1642287423 scopus 로고    scopus 로고
    • Dimerization of TonB is not essential for its binding to the outer membrane siderophore receptor FhuA of Escherichia coli
    • Koedding J, Howard P, Kaufmann L et al. (2004) Dimerization of TonB is not essential for its binding to the outer membrane siderophore receptor FhuA of Escherichia coli. J Biol Chem 279:9978-9986
    • (2004) J Biol Chem , vol.279 , pp. 9978-9986
    • Koedding, J.1    Howard, P.2    Kaufmann, L.3
  • 29
    • 13244255594 scopus 로고    scopus 로고
    • Crystal structure of a 92-residue C-terminal fragment of TonB from Escherichia coli reveals significant conformational changes compared to structures of smaller TonB fragments
    • Koedding J, Killig F, Polzer P et al. (2005) Crystal structure of a 92-residue C-terminal fragment of TonB from Escherichia coli reveals significant conformational changes compared to structures of smaller TonB fragments. J Biol Chem 280:3022-3028
    • (2005) J Biol Chem , vol.280 , pp. 3022-3028
    • Koedding, J.1    Killig, F.2    Polzer, P.3
  • 30
    • 0038385104 scopus 로고    scopus 로고
    • In vivo evidence of TonB shuttling between the cytoplasmic and outer membrane in Escherichia coli
    • Larsen RA, Letain TE, Postle K (2003) In vivo evidence of TonB shuttling between the cytoplasmic and outer membrane in Escherichia coli. Mol Microbiol 49:211-218
    • (2003) Mol Microbiol , vol.49 , pp. 211-218
    • Larsen, R.A.1    Letain, T.E.2    Postle, K.3
  • 31
    • 0035896546 scopus 로고    scopus 로고
    • Conserved residues Ser(16) and His(20) and their relative positioning are essential for TonB activity, cross-linking of TonB with ExbB, and the ability of TonB to respond to proton motive force
    • Larsen RA, Postle K (2001) Conserved residues Ser(16) and His(20) and their relative positioning are essential for TonB activity, cross-linking of TonB with ExbB, and the ability of TonB to respond to proton motive force. J Biol Chem 276:8111-8117
    • (2001) J Biol Chem , vol.276 , pp. 8111-8117
    • Larsen, R.A.1    Postle, K.2
  • 32
    • 0027730652 scopus 로고
    • The conserved proline-rich motif is not essential for energy transduction by Escherichia coli TonB protein
    • Larsen RA, Wood GE, Postle K (1993) The conserved proline-rich motif is not essential for energy transduction by Escherichia coli TonB protein. Mol Microbiol 10:943-953
    • (1993) Mol Microbiol , vol.10 , pp. 943-953
    • Larsen, R.A.1    Wood, G.E.2    Postle, K.3
  • 33
    • 0030943591 scopus 로고    scopus 로고
    • TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Escherichia coli
    • Letain TE, Postle K (1997) TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Escherichia coli. Mol Microbiol 24:271-283
    • (1997) Mol Microbiol , vol.24 , pp. 271-283
    • Letain, T.E.1    Postle, K.2
  • 34
    • 0000046526 scopus 로고    scopus 로고
    • Filamentous phage infection: Crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA
    • Lubkowski J, Hennecke F, Pluckthun A, Wlodawer A (1999) Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA. Structure Fold Des 7:711-722
    • (1999) Structure Fold des , vol.7 , pp. 711-722
    • Lubkowski, J.1    Hennecke, F.2    Pluckthun, A.3    Wlodawer, A.4
  • 36
    • 33744791187 scopus 로고    scopus 로고
    • Structure of TonB in complex with FhuA, E. coli outer membrane receptor
    • Pawelek PD, Croteau N, Ng-Thow-Hing C et al. (2006) Structure of TonB in complex with FhuA, E. coli outer membrane receptor. Science 312:1399-1402
    • (2006) Science , vol.312 , pp. 1399-1402
    • Pawelek, P.D.1    Croteau, N.2    Ng-Thow-Hing, C.3
  • 37
    • 11844269327 scopus 로고    scopus 로고
    • The solution structure of the C-terminal domain of TonB and interaction studies with TonB box peptides
    • Peacock RS, Weljie AM, Howard SP, Price FD, Vogel HJ (2005) The solution structure of the C-terminal domain of TonB and interaction studies with TonB box peptides. J Mol Biol 345:1185-1197
    • (2005) J Mol Biol , vol.345 , pp. 1185-1197
    • Peacock, R.S.1    Weljie, A.M.2    Howard, S.P.3    Price, F.D.4    Vogel, H.J.5
  • 38
    • 0042065285 scopus 로고    scopus 로고
    • Touch and go: Tying TonB to transport
    • Postle K, Kadner RJ (2003) Touch and go: tying TonB to transport. Mol Microbiol 49:869-882
    • (2003) Mol Microbiol , vol.49 , pp. 869-882
    • Postle, K.1    Kadner, R.J.2
  • 39
    • 0033759220 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic bacteria
    • Ratledge C, Dover LG (2000) Iron metabolism in pathogenic bacteria. Annu Rev Microbiol 54:881-941
    • (2000) Annu Rev Microbiol , vol.54 , pp. 881-941
    • Ratledge, C.1    Dover, L.G.2
  • 40
    • 0025992835 scopus 로고
    • Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions
    • Roof SK, Allard JD, Bertrand KP, Postle K (1991) Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions. J Bacteriol 173:5554-5557
    • (1991) J Bacteriol , vol.173 , pp. 5554-5557
    • Roof, S.K.1    Allard, J.D.2    Bertrand, K.P.3    Postle, K.4
  • 41
    • 0141727626 scopus 로고    scopus 로고
    • In vivo evidence for TonB dimerization
    • Sauter A, Howard SP, Braun V (2003) In vivo evidence for TonB dimerization. J Bacteriol 185:5747-5754
    • (2003) J Bacteriol , vol.185 , pp. 5747-5754
    • Sauter, A.1    Howard, S.P.2    Braun, V.3
  • 42
    • 0035136784 scopus 로고    scopus 로고
    • The two TonB systems of Vibrio cholerae: Redundant and specific functions
    • Seliger SS, Mey AR, Valle AM, Payne SM (2001) The two TonB systems of Vibrio cholerae: redundant and specific functions. Mol Microbiol 39:801-812
    • (2001) Mol Microbiol , vol.39 , pp. 801-812
    • Seliger, S.S.1    Mey, A.R.2    Valle, A.M.3    Payne, S.M.4
  • 43
    • 33744780736 scopus 로고    scopus 로고
    • Outer membrane active transport: Structure of the BtuB:TonB complex
    • Shultis DD, Purdy MD, Banchs CN, Wiener MC (2006) Outer membrane active transport: structure of the BtuB:TonB complex. Science 312:1396-1399
    • (2006) Science , vol.312 , pp. 1396-1399
    • Shultis, D.D.1    Purdy, M.D.2    Banchs, C.N.3    Wiener, M.C.4
  • 44
    • 9244255835 scopus 로고    scopus 로고
    • Two tonB systems function in iron transport in Vibrio anguillarum, but only one is essential for virulence
    • Stork M, Di Lorenzo M, Mourino S et al. (2004) Two tonB systems function in iron transport in Vibrio anguillarum, but only one is essential for virulence. Infect Immun 72:7326-7329
    • (2004) Infect Immun , vol.72 , pp. 7326-7329
    • Stork, M.1    Di Lorenzo, M.2    Mourino, S.3
  • 45
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25:4876-4882
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 46
    • 0034818457 scopus 로고    scopus 로고
    • TonB-dependent systems of uropathogenic Escherichia coli: Aerobactin and heme transport and TonB are required for virulence in the mouse
    • Torres AG, Redford P, Welch RA, Payne SM (2001) TonB-dependent systems of uropathogenic Escherichia coli: aerobactin and heme transport and TonB are required for virulence in the mouse. Infect Immun 69:6179-6185
    • (2001) Infect Immun , vol.69 , pp. 6179-6185
    • Torres, A.G.1    Redford, P.2    Welch, R.A.3    Payne, S.M.4
  • 47
    • 0021356806 scopus 로고
    • Iron withholding: A defense against infection and neoplasia
    • Weinberg ED (1984) Iron withholding: a defense against infection and neoplasia. Physiol Rev 64:65-102
    • (1984) Physiol Rev , vol.64 , pp. 65-102
    • Weinberg, E.D.1
  • 48
    • 23044489264 scopus 로고    scopus 로고
    • TonB-dependent outer membrane transport: Going for Baroque?
    • Wiener MC (2005) TonB-dependent outer membrane transport: going for Baroque? Curr Opin Struct Biol 15:394-400
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 394-400
    • Wiener, M.C.1
  • 49
    • 0037102135 scopus 로고    scopus 로고
    • Structure of the periplasmic domain of Pseudomonas aeruginosa TolA: Evidence for an evolutionary relationship with the TonB transporter protein
    • Witty M, Sanz C, Shah A et al. (2002) Structure of the periplasmic domain of Pseudomonas aeruginosa TolA: evidence for an evolutionary relationship with the TonB transporter protein. EMBO J 21:4207-4218
    • (2002) EMBO J , vol.21 , pp. 4207-4218
    • Witty, M.1    Sanz, C.2    Shah, A.3
  • 50
    • 0035087954 scopus 로고    scopus 로고
    • A web-based program for the prediction of average hydropathy, average amphipathicity and average similarity of multiply aligned homologous proteins
    • Zhai Y, Saier MH Jr. (2001) A web-based program for the prediction of average hydropathy, average amphipathicity and average similarity of multiply aligned homologous proteins. J Mol Microbiol Biotechnol 3:285-286
    • (2001) J Mol Microbiol Biotechnol , vol.3 , pp. 285-286
    • Zhai, Y.1    Saier Jr., M.H.2
  • 51
    • 0036185882 scopus 로고    scopus 로고
    • Mutational analysis of the TonB1 energy coupler of Pseudomonas aeruginosa
    • Zhao Q, Poole K (2002) Mutational analysis of the TonB1 energy coupler of Pseudomonas aeruginosa. J Bacteriol 184:1503-1513
    • (2002) J Bacteriol , vol.184 , pp. 1503-1513
    • Zhao, Q.1    Poole, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.